Berberine has gained much attention in recent years owing to its multiple biochemical and pharmacological effects, including anticancer, antiviral, and antibacterial activities. The interaction profile of complex  obtained on molecular docking using Glide module of Maestro Suite indicates berberine interacts at phenylvaline and valine residues of protein and has hydrophobic, non polar interaction and non-covalent interaction via hydrogen bonding at the mentioned active site residues of protein. The protein-ligand complex stability by performing molecular dynamics simulation run of the complex for 100 ps using MacroModel module of Schrodinger suite showed that the complex is stable with time evolution. The in silico study of protein-berberine complex rendered clear picture of interaction of berberine with the protein. Further detailed study of various derivatives of Berberine with protein might lead to more potent and novel class of PKC inhibitors.